2000
DOI: 10.1128/jb.182.22.6366-6373.2000
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Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

Abstract: The role of the carboxy terminus of the Escherichia coli cell division protein FtsA in bacterial division has been studied by making a series of short sequential deletions spanning from residue 394 to 420. Deletions as short as 5 residues destroy the biological function of the protein. Residue W415 is essential for the localization of the protein into septal rings. Overexpression of the ftsA alleles harboring these deletions caused a coiled cell phenotype previously described for another carboxy-terminal mutat… Show more

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Cited by 58 publications
(101 citation statements)
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References 38 publications
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“…FtsZ is able to polymerize to form a ring at the cell center (3,38), and the C-terminal cytosolic domain of FtsZ has been shown to associate with ZipA and FtsA (24,26,32,34,44). Moreover, FtsA is able to dimerize (9,46). Characterization of the interactions involving the other Fts proteins has been limited, probably because these proteins are membrane bound and some of them are expressed at very low levels.…”
mentioning
confidence: 99%
“…FtsZ is able to polymerize to form a ring at the cell center (3,38), and the C-terminal cytosolic domain of FtsZ has been shown to associate with ZipA and FtsA (24,26,32,34,44). Moreover, FtsA is able to dimerize (9,46). Characterization of the interactions involving the other Fts proteins has been limited, probably because these proteins are membrane bound and some of them are expressed at very low levels.…”
mentioning
confidence: 99%
“…The phosphorylation state of FtsA appears to correlate with ATP binding and membrane association, but a mutation that prevents phosphorylation and in vitro ATP binding still rescues conditional ftsA alleles (122). FtsA is part of the actin/hexokinase/HSP70 superfamily (139) and has been shown to dimerize (34,152), but to date there is no evidence that it polymerizes. MreB, a protein required for maintaining cell shape, is a better candidate for a functional prokaryotic homolog of actin (54,138).…”
Section: Stabilizing Proteinsmentioning
confidence: 99%
“…In consequence, a role as a central hub to integrate signals that modulate divisome assembly in E. coli has been assigned to this C-terminal end of FtsZ (53). In (56,57). The ATPase activity of FtsA has not been firmly established, perhaps because its hydrolytic activity is low and an unidentified cofactor is required in vivo for its full activation.…”
Section: The Proto-ring: the Scaffold Of The Divisomementioning
confidence: 99%
“…In (55). The self-interaction of FtsA is essential for the E. coli division process (56,57). The ATPase activity of FtsA has not been firmly established, perhaps because its hydrolytic activity is low and an unidentified cofactor is required in vivo for its full activation.…”
Section: The Proto-ring: the Scaffold Of The Divisomementioning
confidence: 99%
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